Conformation of thymosin beta 4 in water determined by NMR spectroscopy.

Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA

European journal of biochemistry1 Dec 1993Cited by 51 (Europe PMC)

PMID8269922DOI10.1111/j.1432-1033.1993.tb18382.xPepBankPUB-08269922

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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study5

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone5

In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Thymosin beta-4 (human).

01LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other
By NMR, thymosin beta‑4 in water lacks a uniquely folded conformation.
In plain wordsIn lab tests, thymosin beta‑4 in water had no single fixed fold.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableFolded conformation in water
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
NMR showed that thymosin beta 4 lacks a uniquely folded conformation in water.
1 context sentence(design, population, supporting numbers)
Summary · context
The conformational preferences of a 43-amino-acid G-actin-binding peptide, thymosin beta 4, in water at 1, 4 and 14 degrees C, and at pH 3.0 and 6.5 were studied by NMR.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-0826992201
02LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other
By NMR, some preferential alpha-helical conformations of thymosin beta‑4 were observed in aqueous solution.
In plain wordsIn lab tests, thymosin beta‑4 in water showed some preference for helical shapes.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicablePreferential alpha-helical conformations
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
However, some preferential alpha-helical conformations of thymosin beta 4 can be observed in aqueous solutions.
1 context sentence(design, population, supporting numbers)
Summary · context
The conformational preferences of a 43-amino-acid G-actin-binding peptide, thymosin beta 4, in water at 1, 4 and 14 degrees C, and at pH 3.0 and 6.5 were studied by NMR.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-0826992202
03LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other
By NMR, residues 5-16 of thymosin beta‑4 showed interactions typical for both beta-strand and alpha-helical conformations.
In plain wordsIn lab tests, the 5-16 segment of thymosin beta‑4 showed signs of both strand-like and helical shapes.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableConformation of segment 5-16
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
The segment at residues 5-16 showed characteristic interactions for conformations in both the beta-strand and alpha-helical regions of the phi-psi space, based on strong C alpha H(i)-NH(i+1) interactions and NH-NH, C alpha H(i)-NH(i+3), and C alpha H(i)-C beta H(i+3) interactions, respectively.
1 context sentence(design, population, supporting numbers)
Summary · context
The conformational preferences of a 43-amino-acid G-actin-binding peptide, thymosin beta 4, in water at 1, 4 and 14 degrees C, and at pH 3.0 and 6.5 were studied by NMR.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-0826992203
04LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other
By NMR at 1-4 degrees C, residues 31-37 of thymosin beta‑4 showed both beta and alpha conformations, forming a less well-defined helix than residues 5-16.
In plain wordsIn lab tests at 1-4 degrees C, the 31-37 segment of thymosin beta‑4 formed a less defined helix than the 5-16 segment.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableConformation of segment 31-37 at 1-4 degrees C
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
At 1-4 degrees C, another segment at residues 31-37 also shows both beta and alpha conformations, forming however a less well-defined helix than the segment at residues 5-16.
1 context sentence(design, population, supporting numbers)
Summary · context
The conformational preferences of a 43-amino-acid G-actin-binding peptide, thymosin beta 4, in water at 1, 4 and 14 degrees C, and at pH 3.0 and 6.5 were studied by NMR.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-0826992204
05LabNot a test of Thymosin beta-4 (human) aloneIn vitro (cell-free)Other
By NMR at 14 degrees C, the helix population at residues 5-16 of thymosin beta‑4 shifted toward random and turn-like structures, and residues 31-37 became a random coil.
In plain wordsIn lab tests at 14 degrees C, thymosin beta‑4 helical parts became more random, and the 31-37 segment became fully random.
Peptide
Thymosin beta-4 (human)
Outcome
Not applicableConformation at 14 degrees C
Study
n: not reported in source
Outcome group
Receptor activity and mechanism · Pharmacology
Source sentences
Summary
At 14 degrees C, the conformational population of the helix at positions 5-16 is shifted more towards the random and turn-like structures, whereas the segment at positions 31-37 becomes exclusively a random coil.
1 context sentence(design, population, supporting numbers)
Summary · context
The conformational preferences of a 43-amino-acid G-actin-binding peptide, thymosin beta 4, in water at 1, 4 and 14 degrees C, and at pH 3.0 and 6.5 were studied by NMR.
In this study, Thymosin beta-4 (human) was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Thymosin beta-4 (human).
Report a problemFND-0826992205

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

Version 2Current
13 Oct 2026, 01:52 UTC
Study results updated
Version 1
12 Oct 2026, 18:17 UTC
First added · source update from Europe PMC

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